Difference between revisions of "3-phosphoglycerate kinase"

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== Rate equation ==
 
== Rate equation ==
  
Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used.<ref name="pmid6765200">{{cite journal |author=Watson HC, Walker NP, Shaw PJ, ''et al.'' |title=Sequence and structure of yeast phosphoglycerate kinase |journal=EMBO J. |volume=1 |issue=12 |pages=1635–40 |year=1982 |pmid=6765200 |pmc=553262 |doi= |url=}}</ref> Since
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Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used.<ref>A book by Harold McGee</ref> Since
  
  

Revision as of 12:03, 27 February 2014

Phosphoglycerate kinase (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Like all kinases it is a transferase.

Chemical equation

 1,3BPG + ADP \rightleftharpoons 3PG + ATP


Rate equation

Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used.[1] Since


 \frac{V_{mf}\frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} }

Parameter values

Alternative parameter values

References

Template:Reflist
  1. A book by Harold McGee